Ubiquitination during Plant Immune Signaling

Marino, Daniel; Peeters, Nemo; Rivas, Susana

doi:10.1104/pp.112.199281

Cited by 184 publications

(169 citation statements)

References 120 publications

(163 reference statements)

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“…In Arabidopsis, 1415 putative E3 ligases have been identified that are expected to allow the interaction between E2 enzymes and target proteins and, among them, 499 RING-type proteins have been predicted 10 . A significant number of UPS-related components, in particular E3 ligases, have been described as being involved in the regulation of plant immunity at all stages from pathogen recognition to downstream signalling, including hormone signalling pathways that regulate plant immune responses [14][15][16] . For example, following perception of bacterial flagellin, the Arabidopsis U-Box proteins PUB12 and PUB13 associate with the immune receptor FLS2, mediating its ubiquitination and degradation and providing an efficient mechanism of attenuation of basal defenses 17 .…”

Section: Discussionmentioning

confidence: 99%

“…Although XB3 is necessary for full accumulation of XA21 and for XA21-mediated resistance in rice, its targets remain to be discovered 20 . The important role of ubiquitination-related processes during the regulation of plant responses to pathogens is underlined by the finding that most microbes appear to have evolved a way to subvert the host UPS to promote disease 14,15 . Ubiquitination has a central role in different aspects of transcriptional regulation in animal cells, including (i) chromatin remodelling via histone modification and (ii) coordination of transcription initiation and elongation via ubiquitination of TFs and RNA polymerase II 21 .…”

Section: Discussionmentioning

confidence: 99%

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Arabidopsis ubiquitin ligase MIEL1 mediates degradation of the transcription factor MYB30 weakening plant defence

et al. 2013

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One of the most efficient plant resistance reactions to pathogen attack is the hypersensitive response, a form of programmed cell death at infection sites. The Arabidopsis transcription factor MYB30 is a positive regulator of hypersensitive cell death responses. Here we show that MIEL1 (MYB30-Interacting E3 Ligase1), an Arabidopsis RING-type E3 ubiquitin ligase that interacts with and ubiquitinates MYB30, leads to MYB30 proteasomal degradation and downregulation of its transcriptional activity. In non-infected plants, MIEL1 attenuates cell death and defence through degradation of MYB30. Following bacterial inoculation, repression of MIEL1 expression removes this negative regulation allowing sufficient MYB30 accumulation in the inoculated zone to trigger the hypersensitive response and restrict pathogen growth. Our work underlines the important role played by ubiquitination to control the hypersensitive response and highlights the sophisticated fine-tuning of plant responses to pathogen attack. Overall, this work emphasizes the importance of protein modification by ubiquitination during the regulation of transcriptional responses to stress in eukaryotic cells.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Arabidopsis ubiquitin ligase MIEL1 mediates degradation of the transcription factor MYB30 weakening plant defence

et al. 2013

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“…Functional characterization suggested redundancy among group III members for their role in the suppression of plant immunity by AvrPtoB and in PTI and identified UBIQUITIN-CONJUGATING11 (UBC11), UBC28, UBC29, UBC39, and UBC40 as playing a more significant role in PTI than other group III members. Our work builds a foundation for the further characterization of E2s in plant immunity and reveals that AvrPtoB has evolved a strategy for suppressing host immunity that is difficult for the plant to thwart.Ubiquitination as a major posttranslational modification of proteins in eukaryotes has emerged in recent years as an important regulatory mechanism underlying plant innate immunity Fu et al, 2012;Marino et al, 2012;Li et al, 2014). The ubiquitination process involves a consecutive, threestep enzymatic cascade that is catalyzed by three different classes of enzymes: ubiquitin-activating (E1), ubiquitin-conjugating (E2), and ubiquitin ligase (E3) enzymes.…”

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confidence: 99%

“…Ubiquitination as a major posttranslational modification of proteins in eukaryotes has emerged in recent years as an important regulatory mechanism underlying plant innate immunity Fu et al, 2012;Marino et al, 2012;Li et al, 2014). The ubiquitination process involves a consecutive, threestep enzymatic cascade that is catalyzed by three different classes of enzymes: ubiquitin-activating (E1), ubiquitin-conjugating (E2), and ubiquitin ligase (E3) enzymes.…”

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confidence: 99%

A Subset of Ubiquitin-Conjugating Enzymes Is Essential for Plant Immunity

et al. 2016

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Of the three classes of enzymes involved in ubiquitination, ubiquitin-conjugating enzymes (E2) have been often incorrectly considered to play merely an auxiliary role in the process, and few E2 enzymes have been investigated in plants. To reveal the role of E2 in plant innate immunity, we identified and cloned 40 tomato genes encoding ubiquitin E2 proteins. Thioester assays indicated that the majority of the genes encode enzymatically active E2. Phylogenetic analysis classified the 40 tomato E2 enzymes into 13 groups, of which members of group III were found to interact and act specifically with AvrPtoB, a Pseudomonas syringae pv tomato effector that uses its ubiquitin ligase (E3) activity to suppress host immunity. Knocking down the expression of group III E2 genes in Nicotiana benthamiana diminished the AvrPtoB-promoted degradation of the Fen kinase and the AvrPtoB suppression of host immunity-associated programmed cell death. Importantly, silencing group III E2 genes also resulted in reduced pattern-triggered immunity (PTI). By contrast, programmed cell death induced by several effector-triggered immunity elicitors was not affected on group III-silenced plants. Functional characterization suggested redundancy among group III members for their role in the suppression of plant immunity by AvrPtoB and in PTI and identified UBIQUITIN-CONJUGATING11 (UBC11), UBC28, UBC29, UBC39, and UBC40 as playing a more significant role in PTI than other group III members. Our work builds a foundation for the further characterization of E2s in plant immunity and reveals that AvrPtoB has evolved a strategy for suppressing host immunity that is difficult for the plant to thwart.Ubiquitination as a major posttranslational modification of proteins in eukaryotes has emerged in recent years as an important regulatory mechanism underlying plant innate immunity Fu et al., 2012;Marino et al., 2012;Li et al., 2014). The ubiquitination process involves a consecutive, threestep enzymatic cascade that is catalyzed by three different classes of enzymes: ubiquitin-activating (E1), ubiquitin-conjugating (E2), and ubiquitin ligase (E3) enzymes. The first step of the process activates ubiquitin, a highly conserved 76-amino acid protein, in an ATP-dependent manner by attaching ubiquitin to an E1 enzyme. The activated ubiquitin is then transferred from the E1 to the Cys residue at the active site of an E2 conjugating enzyme. An E3 ligase then recruits the substrate protein to the E2 to transfer the ubiquitin molecule from E2 to the substrate. Through the action of E1, E2, and E3, ubiquitin is covalently attached usually to the Lys residue of a substrate through an isopeptide bond (Hershko and Ciechanover, 1998). Of the three enzymes involved in ubiquitination, E3 ubiquitin ligases have been the focus of many studies due to their key role in determining substrate specificity for the ubiquitination

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“…5). Ubiquitination has been shown to be involved in other plant PCD examples such as leaf senescence (Pinedo et al 1996;Wang et al 2014) and hypersensitive response (Marino et al 2012). During daylily leaf senescence, ubiquitin and ubiquitin conjugates have been shown to increase (Courtney et al 1994).…”

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confidence: 99%

Identification of Differentially Expressed Genes during Lace Plant Leaf Development

Rantong

Kelen

Breusegem

et al. 2016

International Journal of Plant Sciences

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Editor: John L. Bowman Premise of research. The lace plant is an excellent and unique model for studying developmentally regulated programmed cell death (PCD) in plants. Perforations form in highly predictable and easily accessible and distinguishable areas in lace plant leaves. However, little is known about the genes involved in regulation of this PCD or leaf development. In this study, for the first time, a general gene expression profile for lace plant leaf development was investigated.Methodology. A cDNA-amplified fragment length polymorphism involving 64 primer combinations was used for a half-genome analysis of 4666 transcripts. Two hundred and thirty differentially expressed transcriptderived fragments (TDFs) were sequenced. A partial expressed sequence tag (EST) database for window-stage (in which PCD is occurring) leaves was also established. Through a reverse transcription polymerase chain reaction, the possible role of ubiquitin in lace plant PCD was investigated.Pivotal results. Seventy-nine TDFs were successfully annotated. The isolated TDFs and ESTs encoded genes involved in processes such as photosynthesis, biosynthesis pathways, gene regulation, stress responses, defense against pathogens, and PCD, among others. Indirect evidence through ubiquitin transcript levels suggests involvement of proteasome machinery in lace plant development and PCD. This study provides a foundation for selective studies on regulation of lace plant leaf development and PCD.

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Ubiquitination during Plant Immune Signaling

Cited by 184 publications

References 120 publications

Arabidopsis ubiquitin ligase MIEL1 mediates degradation of the transcription factor MYB30 weakening plant defence

Arabidopsis ubiquitin ligase MIEL1 mediates degradation of the transcription factor MYB30 weakening plant defence

A Subset of Ubiquitin-Conjugating Enzymes Is Essential for Plant Immunity

Identification of Differentially Expressed Genes during Lace Plant Leaf Development

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